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Database: UniProt
Entry: M3JT38_CANMX
LinkDB: M3JT38_CANMX
Original site: M3JT38_CANMX 
ID   M3JT38_CANMX            Unreviewed;       625 AA.
AC   M3JT38;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Malic enzyme {ECO:0000313|EMBL:EMG46005.1};
GN   ORFNames=G210_3765 {ECO:0000313|EMBL:EMG46005.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG46005.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG46005.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG46005.1}.
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DR   EMBL; AOGT01002203; EMG46005.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3JT38; -.
DR   STRING; 1245528.M3JT38; -.
DR   eggNOG; KOG1257; Eukaryota.
DR   HOGENOM; CLU_011405_5_2_1; -.
DR   OMA; YYRMLME; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT   DOMAIN          124..305
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          315..568
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        219
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         290
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         291
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         314
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         459
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         499
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   625 AA;  69455 MW;  B35ED56336091F1A CRC64;
     MTVVASRQPT IRRTSIVVDT DSPNIKCIKT PIGDTAETEF LLPKATRLSM DGPVECVLTG
     FALLNSPQFN KGSAFTEEER ISFELVGLLP AKVNSLDEQV ERSYQQFTYL KSPLAKNDFC
     TSMRLQNKVL YYELVRRHIR EMLPIIYTPT EGDAIMNYSE RFRKPEGCFL DINDPGSIDR
     RLASFGKDKD IDYIVMSDGE GILGIGDQGV GAIRIAIAKL GLMTLCGGIH PARVLPIGLD
     VGTNNERLLN DDIYMGNKFS RVRGERYWGF IDQVIKSIKH RFPSAVLHYE DFGVSTGRDM
     LHKYREFLPS FNDDIQGTGA VVMASITAAL KFSKRDLKNI QVLIYGAGSA GLGIADQITN
     HLISHGLTPT EAKSRIHCMD RFGLITDKST KEASPAQMLY ADPSSEWDGV DTKSLLECVK
     KIKPTVLVGC STQPGAFTEE IVKAMYAHNP QPIIFPLSNP TRLHEAKPVD LMKWTDNNAL
     VATGSPFEPV DGYEISENNN CFTFPGIGLG AVLSRCTTIS DTMISAAVDR LAEMSPKMEN
     EKCGLLPDLE DINDVSANVA TAVILQAFKE GKARIELEKK PDGGLVSVPK NYDDCLEWVK
     SQMWRPVYRP YVKVQYVSNI HTYQY
//
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